%0 Journal Article %T The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors %+ Institut de Génétique et Développement de Rennes (IGDR) %A Macé, Kevin %A Giudice, Emmanuel %A Chat, Sophie %A Gillet, Reynald %Z Netherlands Organization for Scientific Research (NOW) %Z European Regional Development Fund of the European Commission %Z French Infrastructure for Integrated Structural Biology (FRISBI) [ANR-10-INSB-05] %Z Agence Nationale de la Recherche [ANR-14-ASTR-0001] %Z University of Rennes 1 %< avec comité de lecture %@ 0305-1048 %J Nucleic Acids Research %I Oxford University Press %V 46 %N 6 %P 3211-3217 %8 2018-02-02 %D 2018 %R 10.1093/nar/gky081 %M 29408956 %Z Life Sciences [q-bio]/GeneticsJournal articles %X During translation's elongation cycle, elongation factor G (EF-G) promotes messenger and transfer RNA translocation through the ribosome. Until now, the structures reported for EF-G-ribosome complexes have been obtained by trapping EF-G in the ribosome. These results were based on use of non-hydrolyzable guanosine 5'-triphosphate (GTP) analogs, specific inhibitors or a mutated EF-G form. Here, we present the first cryo-electron microscopy structure of EF-G bound to ribosome in the absence of an inhibitor. The structure reveals a natural conformation of EF-G.GDP in the ribosome, with a previously unseen conformation of its third domain. These data show how EF-G must affect translocation, and suggest the molecular mechanism by which fusidic acid antibiotic prevents the release of EF-G after GTP hydrolysis. %G English %2 https://univ-rennes.hal.science/hal-01795396/document %2 https://univ-rennes.hal.science/hal-01795396/file/gky081.pdf %L hal-01795396 %U https://univ-rennes.hal.science/hal-01795396 %~ UNIV-RENNES1 %~ CNRS %~ IFR140 %~ IGDR %~ STATS-UR1 %~ IGDR-TR %~ GENCI %~ UR1-UFR-SVE %~ UR1-HAL %~ UR1-SDV %~ TEST-UR-CSS %~ UNIV-RENNES %~ TEST-HALCNRS %~ ANR %~ UR1-BIO-SA